Achieving efficient water management at the Federal University of São Paulo, Brazil

In 2015, the water crisis affecting the São Paulo Metropolitan Region reached its peak. The Federal Government published an Ordinance stablishing good practices in the management and use of water and electricity. This work aimed to verify if the management actions performed at the Universidade Federal de São Paulo were effective for water consumption reduction. It was analyzed secondary data of the monthly water consumption at campuses and Rectory, from 2014 to 2016. Statistical analyses were carried out comparing the water consumption between the periods pre- and post-intervention, which occurred in February 2015. The results show that the intervention reduced per capita water consumption by 33% in 2015 and 35% in 2016, saving up more than 65,000 m3 of water. These management actions were effective, and helped the academic population to achieve a more efficiently use of water and financial resources, becoming more sustainable.In 2015, the water crisis affecting the São Paulo Metropolitan Region reached its peak. The Federal Government published an Ordinance establishing good practices in the management and use of water and electricity. This work aims to verify if management actions performed at the Federal University of São Paulo were effective for water consumption reduction. We assessed measures such as awareness campaigns, water reuse, water pressure regulator installation, identification of leaks, irrigation and washing of floors reduction. It was analyzed secondary data of the monthly water consumption at campuses and Rectory, from 2014 to 2016. Statistical analyses were carried out comparing the water consumption between the pre and post-intervention periods, which occurred in February 2015. The results show that the intervention reduced per capita water consumption by 33% in 2015 and 35% in 2016, saving up more than 65,000 m3 of water. These management actions proved to be effective, and the academic population achieved a more efficient use of water and financial resources, becoming more sustainable

Protease inhibitors extracted from caesalpinia echinata lam. Affect kinin release during lung inflammation

Inflammation is an essential process in many pulmonary diseases in which kinins are generated by protease action on kininogen, a phenomenon that is blocked by protease inhibitors. We evaluated kinin release in an in vivo lung inflammation model in rats, in the presence or absence of CeKI (C. echinata kallikrein inhibitor), a plasma kallikrein, cathepsin G, and proteinase-3 inhibitor, and rCeEI (recombinant C. echinata elastase inhibitor), which inhibits these proteases and also neutrophil elastase. Wistar rats were intravenously treated with buffer (negative control) or inhibitors and, subsequently, lipopolysaccharide was injected into their lungs. Blood, bronchoalveolar lavage fluid (BALF), and lung tissue were collected. In plasma, kinin release was higher in the LPS-treated animals in comparison to CeKI or rCeEI groups. rCeEI-treated animals presented less kinin than CeKI-treated group. Our data suggest that kinins play a pivotal role in lung inflammation and may be generated by different enzymeshowever, neutrophil elastase seems to be the most important in the lung tissue context. These results open perspectives for a better understanding of biological process where neutrophil enzymes participate and indicate these plant inhibitors and their recombinant correlates for therapeutic trials involving pulmonary diseases.Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [04/11015-0, 07/55496-0, 01/02457-0]Conselho Nacional de Desenvolvimento Cientifico e Tecnologico [304923/2006-0, 304719/2009-9]Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior/Ministerio da Educacao Superior de Cuba (CAPES/MES), Brazil [011/06, 077/09]Department of Biochemistry, Universidade Federal de S˜ao Paulo, Rua Trˆes de Maio, No. 100, 04044-020 S˜ao Paulo, SP, BrazilSchool of Arts, Sciences and Humanities, Universidade de São Paulo, Avenida Arlindo Bettio, No. 1000, 03828-000 São Paulo, SP, BrazilDepartment of Marine Sciences, Universidade Federal de São Paulo, Rua Doutor Carvalho de Mendonça, No. 144, 11070-100 Santos, SP, BrazilJapan Health Care College, Sinei 434-1, Kiyota-ku, Sapporo, JapanDepartment of Marine Sciences, Universidade Federal de São Paulo, Rua Doutor Carvalho de Mendonça, No. 144, 11070-100 Santos, SP, BrazilFAPESP: 04/11015-0FAPESP: 07/55496-0FAPESP: 01/02457-0CNPq: 304923/2006-0CNPq: 304719/2009-9CAPES/MES: 011/06 and 077/09Web of Scienc

Antioxidant dietary deficiency induces caspase activation in chick skeletal muscle cells

Apoptosis and necrosis are two distinct forms of cell death that can occur in response to different agents and stress conditions. In order to verify if the oxidative stress induced by dietary selenium and vitamin E deficiencies can lead muscle cells to apoptosis, one-day-old chicks were reared using diets differing in their vitamin E (0 or 10 IU/kg) and selenium (0 or 0.15 ppm) supplementation. Chick skeletal muscle tissue was obtained from 28-day-old animals and used to verify apoptosis occurrence based on caspase activity detection and DNA fragmentation. Antioxidant deficiency significantly increased caspase-like activity assessed by the hydrolysis of fluorogenic peptide substrates (Abz-peptidyl-EDDnp) at lambdaexc = 320 nm and lambdaem = 420 nm. Proteolytic activation was not accompanied by typical internucleosomal DNA fragmentation detected by field inversion gel electrophoresis. Although the general caspase inhibitor N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone (Z-VAD-fmk) (0 to 80 muM) did not block caspase-like activity when preincubated for 30 min with muscle homogenates, the hydrolyzed substrates presented the same cleavage profile in HPLC (at the aspartic acid residue) when incubated with the purified recombinant enzyme caspase-3. These data indicate that oxidative stress causes caspase-like activation in muscle cells and suggest that cell death associated with exudative diathesis (dietary deficiency of selenium and vitamin E) can follow the apoptotic pathway.Universidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BioquímicaUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BiofísicaUniversidade de São Paulo Faculdade de Zootecnia e Engenharia de Alimentos Departamento de CiênciasUNIFESP, EPM, Depto. de BioquímicaUNIFESP, EPM, Depto. de BiofísicaSciEL

Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors

Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 µM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 µM) activation. On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 µM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin and heparan sulfate increased (1.4 times) the enzyme inhibition by the C1-inhibitor (150 nM).Universidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BioquímicaUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BiofísicaUNIFESP, EPM, Depto. de BioquímicaUNIFESP, EPM, Depto. de BiofísicaSciEL

Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins

Several proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds of Caesalpinia echinata Lam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatographies and gel filtration. This 61-kDa serine protease (CeSP) hydrolyses H-D-prolyl-L-phenylalanyl-L-arginine-p-nitroanilide (Km 55.7 μM) in an optimum pH of 7.1, and this activity is effectively retained until 50°C. CeSP remained stable in the presence of kosmotropic anions (PO4 3−, SO4 2−, and CH3COO−) or chaotropic cations (K+ and Na+). It is strongly inhibited by TLCK, a serine protease inhibitor, but not by E-64, EDTA or pepstatin A. The characteristics of the purified enzyme allowed us to classify it as a serine protease. The role of CeSP in the seeds cannot be assigned yet but is possible to infer that it is involved in the mobilization of seed storage proteins

Educomunicação em Tempos de Pandemia:

Os textos que compõem esta obra são oriundos do VIII Colóquio Ibero-americano de Educomunicação (VIII CIEducom) e IX Colóquio Catarinense de Educomunicação (IX CCEducom), realizados em março de 2021. Em um ano no qual o vírus SARS-CoV-2 e variantes circularam por diversos territórios, Educomunicação em tempos de pandemia: práticas e desafios foi o tema discutido nos eventos. Este livro colocado à disposição do público é um modo de compartilhar caminhos e convidar pessoas curiosas a percorrerem, por meio das palavras e recursos gráficos, desafios identificados e estratégias para o enfrentamento deste inesperado período de pandemia